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Showing 1–8 of 8 results
Advanced filters: Author: Richard Obexer Clear advanced filters

  • Nucleoside triphosphates (NTPs) are important building blocks that underpin emerging enzymatic approaches to RNA therapeutics manufacturing. Here, authors develop a biocatalytic strategy to convert nucleosides into NTPs containing clinically relevant modifications, using simple phosphate donors.

    • Qinglong Meng
    • Caecilie Benckendorff
    • Sarah L. Lovelock
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-11

  • Directed evolution typically requires extensive screening. This work presents an ultrahigh-throughput microfluidic assay, based on a coupled reaction and fluorescence-activated droplet sorting, enabling a 960-fold activity improvement of an amine oxidase for a non-natural substrate in a single round.

    • Aaron Debon
    • Moritz Pott
    • Donald Hilvert
    Research
    Nature Catalysis
    Volume: 2, P: 740-747

  • Phase separation is being revealed as important in many biological processes. Most attempts to mimic and deconstruct this use engineered natural proteins. Now it is shown that de novo proteins can be designed from first principles to undergo liquid–liquid phase separation in cells, with the potential to organize multi-enzyme pathways.

    • Alexander T. Hilditch
    • Andrey Romanyuk
    • Derek N. Woolfson
    ResearchOpen Access
    Nature Chemistry
    Volume: 16, P: 89-97

  • Recent studies have shown that energy transfer photoenzymes can be engineered to promote stereocontrolled [2 + 2] cycloadditions; however, existing systems rely on ultraviolet light and display limited photochemical efficiencies. A generation of thioxanthone-containing photoenzymes now harnesses visible light to drive challenging photochemical conversions with high efficiencies and selectivities.

    • Rebecca Crawshaw
    • Ross Smithson
    • Anthony P. Green
    ResearchOpen Access
    Nature Chemistry
    Volume: 17, P: 1083-1090

  • An artificial aldolase has been optimized using an ultrahigh-throughput microfluidic screening assay. The evolved enzyme exhibits excellent stereoselectivity and broad substrate scope. Structural studies suggest that a Lys-Tyr-Asn-Tyr catalytic tetrad, which emerged during directed evolution, is responsible for the >109 rate enhancement achieved by this catalyst.

    • Richard Obexer
    • Alexei Godina
    • Donald Hilvert
    Research
    Nature Chemistry
    Volume: 9, P: 50-56

  • The authors previously showed that a histidine nucleophile and a flexible arginine can work in synergy to accelerate the Morita Baylis-Hillman (MBH) reaction. Here, they report another efficient MBHase that employs a non-canonical Nδ-methylhistidine nucleophile paired with a catalytic glutamate, providing an alternative mechanistic solution for MBH catalysis.

    • Amy E. Hutton
    • Jake Foster
    • Anthony P. Green
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-13

  • A previously designed enzyme used a reactive lysine to initiate cleavage of a carbon-carbon bond. Directed evolution of this construct now shows a drastic reorganization of the active site to use an alternative catalytic lysine and suggests considerations for future design efforts.

    • Lars Giger
    • Sami Caner
    • Donald Hilvert
    Research
    Nature Chemical Biology
    Volume: 9, P: 494-498

  • A genetically encoded triplet photosensitizer is used to develop an efficient photoenzyme that can promote enantioselective intramolecular and bimolecular [2+2] cycloadditions by means of triplet energy transfer.

    • Jonathan S. Trimble
    • Rebecca Crawshaw
    • Anthony P. Green
    Research
    Nature
    Volume: 611, P: 709-714